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Database: PDB
Entry: 4G5G
LinkDB: 4G5G
Original site: 4G5G 
HEADER    TRANSLATION/ANTIBIOTIC                  17-JUL-12   4G5G              
TITLE     EF-TU (ESCHERICHIA COLI) COMPLEXED WITH NVP-LDU796                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ELONGATION FACTOR TU 1;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: EF-TU 1, P-43;                                              
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: THIOMURACIN A DERIVATIVE;                                  
COMPND   8 CHAIN: I;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K12;                                                         
SOURCE   5 GENE: TUFA, B3339, JW3301;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  11 ORGANISM_TAXID: 32630                                                
KEYWDS    ELONGATION FACTOR, TRANSLATION-ANTIBIOTIC COMPLEX                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.PALESTRANT                                                          
REVDAT   1   26-DEC-12 4G5G    0                                                
JRNL        AUTH   M.J.LAMARCHE,J.A.LEEDS,J.DZINK-FOX,E.GANGL,P.KRASTEL,        
JRNL        AUTH 2 G.NECKERMANN,D.PALESTRANT,M.A.PATANE,E.M.RANN,S.TIAMFOOK,    
JRNL        AUTH 3 D.YU                                                         
JRNL        TITL   ANTIBIOTIC OPTIMIZATION AND CHEMICAL STRUCTURE STABILIZATION 
JRNL        TITL 2 OF THIOMURACIN A.                                            
JRNL        REF    J.MED.CHEM.                   V.  55  6934 2012              
JRNL        REFN                   ISSN 0022-2623                               
JRNL        PMID   22812377                                                     
JRNL        DOI    10.1021/JM300783C                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNX                                                  
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21195                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.212                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 952                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT/AGREEMENT OF MODEL WITH ALL DATA.                               
REMARK   3   R VALUE     (WORKING + TEST SET, NO CUTOFF) : NULL                 
REMARK   3   R VALUE            (WORKING SET, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE                    (NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET SIZE   (%, NO CUTOFF) : NULL                 
REMARK   3   FREE R VALUE TEST SET COUNT     (NO CUTOFF) : NULL                 
REMARK   3   ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL                 
REMARK   3   TOTAL NUMBER OF REFLECTIONS     (NO CUTOFF) : 21195                
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : NULL                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : NULL                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3099                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 117                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.009                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.60                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4G5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB073761.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-MAR-07                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.23                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.00000                            
REMARK 200  MONOCHROMATOR                  : SI                                 
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21195                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1D8T                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 50.85                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.2M MGSO4, 24% PEG3350 ,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 8.23            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       40.15250            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       61.78850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.15250            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       61.78850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 MG    MG A 503  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 689  LIES ON A SPECIAL POSITION.                          
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400                                                                      
REMARK 400 THE THIOMURACIN A DERIVATIVE IS OLIGOPEPTIDE, A MEMBER OF            
REMARK 400 ANTIBIOTIC CLASS.                                                    
REMARK 400                                                                      
REMARK 400  GROUP: 1                                                            
REMARK 400   NAME: THIOMURACIN A DERIVATIVE                                     
REMARK 400   CHAIN: I                                                           
REMARK 400   COMPONENT_1: PEPTIDE LIKE POLYMER                                  
REMARK 400   DESCRIPTION: NULL                                                  
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     0                                                      
REMARK 465     ALA A     1                                                      
REMARK 465     LYS A     2                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO A 128   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500    TYR I 906   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    TYR I 906   CG  -  CD2 -  CE2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A   4       43.25    -98.69                                   
REMARK 500    ALA A  57      -77.96    -89.35                                   
REMARK 500    ASP A 142       75.61    -68.51                                   
REMARK 500    GLU A 143      -13.04    -42.46                                   
REMARK 500    ASP A 181      102.99    -53.21                                   
REMARK 500    GLU A 215      -77.29   -107.63                                   
REMARK 500    SER A 221      118.01    -38.78                                   
REMARK 500    ILE A 247      -68.95     66.02                                   
REMARK 500    ARG A 262       -1.27     74.94                                   
REMARK 500    ARG A 333      -83.59     60.80                                   
REMARK 500    H14 I 904      -32.77   -138.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 690        DISTANCE =  5.90 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 501  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A  25   OG1                                                    
REMARK 620 2 GDP A 502   O2B  80.5                                              
REMARK 620 3 HOH A 615   O   171.9  92.0                                        
REMARK 620 4 HOH A 601   O    79.0  81.2  96.8                                  
REMARK 620 5 HOH A 602   O    83.7  84.3  98.8 159.0                            
REMARK 620 6 HOH A 616   O    82.9 163.2 104.7  98.4  91.1                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 503  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 654   O                                                      
REMARK 620 2 HOH A 653   O   101.6                                              
REMARK 620 3 HOH A 681   O   113.0  84.2                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF THIOMURACIN A          
REMARK 800  DERIVATIVE                                                          
DBREF  4G5G A    2   393  UNP    P0CE47   EFTU1_ECOLI      3    394             
DBREF  4G5G I  900   912  PDB    4G5G     4G5G           900    912             
SEQADV 4G5G MET A    0  UNP  P0CE47              EXPRESSION TAG                 
SEQADV 4G5G ALA A    1  UNP  P0CE47              EXPRESSION TAG                 
SEQRES   1 A  394  MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL          
SEQRES   2 A  394  ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR          
SEQRES   3 A  394  THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR          
SEQRES   4 A  394  TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN          
SEQRES   5 A  394  ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR          
SEQRES   6 A  394  SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA          
SEQRES   7 A  394  HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN          
SEQRES   8 A  394  MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU          
SEQRES   9 A  394  VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG          
SEQRES  10 A  394  GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR          
SEQRES  11 A  394  ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP          
SEQRES  12 A  394  GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU          
SEQRES  13 A  394  LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO          
SEQRES  14 A  394  ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP          
SEQRES  15 A  394  ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE          
SEQRES  16 A  394  LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP          
SEQRES  17 A  394  LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE          
SEQRES  18 A  394  SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG          
SEQRES  19 A  394  GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY          
SEQRES  20 A  394  ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU          
SEQRES  21 A  394  MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU          
SEQRES  22 A  394  ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU          
SEQRES  23 A  394  ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE          
SEQRES  24 A  394  LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU          
SEQRES  25 A  394  SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS          
SEQRES  26 A  394  GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL          
SEQRES  27 A  394  THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL          
SEQRES  28 A  394  MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE          
SEQRES  29 A  394  HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE          
SEQRES  30 A  394  ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA          
SEQRES  31 A  394  LYS VAL LEU GLY                                              
SEQRES   1 I   13  SER BB9 ASN BB6 H14 BB9 TYR 05N BB9 BB9 MH6 BB9 NH2          
MODRES 4G5G BB9 I  901  CYS                                                     
MODRES 4G5G BB6 I  903  CYS  (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID            
MODRES 4G5G H14 I  904  PHE  (2S,3R)-BETA-HYDROXY-PHENYLALANINE                 
MODRES 4G5G BB9 I  905  CYS                                                     
MODRES 4G5G 05N I  907  PRO  (3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE               
MODRES 4G5G BB9 I  908  CYS                                                     
MODRES 4G5G BB9 I  909  CYS                                                     
MODRES 4G5G MH6 I  910  SER  3-HYDROXY-2-IMINOPROPANOIC ACID                    
MODRES 4G5G BB9 I  911  CYS                                                     
HET    BB9  I 901       6                                                       
HET    BB6  I 903       7                                                       
HET    H14  I 904      11                                                       
HET    BB9  I 905       6                                                       
HET    05N  I 907       8                                                       
HET    BB9  I 908       5                                                       
HET    BB9  I 909       5                                                       
HET    MH6  I 910       4                                                       
HET    BB9  I 911       6                                                       
HET    NH2  I 912       1                                                       
HET     MG  A 501       1                                                       
HET    GDP  A 502      28                                                       
HET     MG  A 503       1                                                       
HET    SO4  A 504       5                                                       
HETNAM     BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID                         
HETNAM     BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID                          
HETNAM     H14 (2S,3R)-BETA-HYDROXY-PHENYLALANINE                               
HETNAM     05N (3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE                             
HETNAM     MH6 3-HYDROXY-2-IMINOPROPANOIC ACID                                  
HETNAM     NH2 AMINO GROUP                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     SO4 SULFATE ION                                                      
HETSYN     H14 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-                
HETSYN   2 H14  PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,            
HETSYN   3 H14  L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-           
HETSYN   4 H14  HYDROXY-L-PHENYLALANINE                                         
FORMUL   2  BB9    5(C3 H5 N O2 S)                                              
FORMUL   2  BB6    C4 H7 N O2 S                                                 
FORMUL   2  H14    C9 H11 N O3                                                  
FORMUL   2  05N    C6 H11 N O3                                                  
FORMUL   2  MH6    C3 H5 N O3                                                   
FORMUL   2  NH2    H2 N                                                         
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   4  GDP    C10 H15 N5 O11 P2                                            
FORMUL   6  SO4    O4 S 2-                                                      
FORMUL   7  HOH   *117(H2 O)                                                    
HELIX    1   1 GLY A   23  GLY A   40  1                                  18    
HELIX    2   2 ALA A   45  ASN A   51  1                                   7    
HELIX    3   3 GLY A   83  GLY A   94  1                                  12    
HELIX    4   4 MET A  112  GLY A  126  1                                  15    
HELIX    5   5 GLU A  144  TYR A  160  1                                  17    
HELIX    6   6 SER A  173  GLU A  179  1                                   7    
HELIX    7   7 ASP A  181  ILE A  199  1                                  19    
HELIX    8   8 ARG A  204  LYS A  208  5                                   5    
SHEET    1   A 6 SER A  65  ASP A  70  0                                        
SHEET    2   A 6 HIS A  75  ASP A  80 -1  O  HIS A  78   N  VAL A  67           
SHEET    3   A 6 HIS A  11  ILE A  17  1  N  VAL A  14   O  ALA A  77           
SHEET    4   A 6 ALA A 101  ALA A 106  1  O  ILE A 102   N  GLY A  15           
SHEET    5   A 6 ILE A 130  ASN A 135  1  O  ILE A 131   N  LEU A 103           
SHEET    6   A 6 ILE A 169  ARG A 171  1  O  VAL A 170   N  VAL A 132           
SHEET    1   B 2 GLU A  54  LYS A  56  0                                        
SHEET    2   B 2 THR A  61  ASN A  63 -1  O  ILE A  62   N  GLU A  55           
SHEET    1   C 7 LEU A 211  PRO A 213  0                                        
SHEET    2   C 7 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   C 7 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   C 7 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5   C 7 ASN A 273  LEU A 278 -1  O  LEU A 277   N  GLY A 257           
SHEET    6   C 7 GLY A 224  ARG A 230 -1  N  VAL A 227   O  VAL A 276           
SHEET    7   C 7 VAL A 217  ILE A 220 -1  N  PHE A 218   O  VAL A 226           
SHEET    1   D 5 LEU A 211  PRO A 213  0                                        
SHEET    2   D 5 VAL A 291  ALA A 293 -1  O  LEU A 292   N  LEU A 212           
SHEET    3   D 5 GLU A 241  VAL A 245 -1  N  GLU A 243   O  ALA A 293           
SHEET    4   D 5 GLN A 251  MET A 260 -1  O  GLN A 251   N  ILE A 244           
SHEET    5   D 5 LYS A 263  LEU A 265 -1  O  LEU A 265   N  VAL A 258           
SHEET    1   E 2 ILE A 235  LYS A 237  0                                        
SHEET    2   E 2 GLU A 267  ARG A 269 -1  O  GLY A 268   N  ILE A 236           
SHEET    1   F 7 LYS A 299  ILE A 310  0                                        
SHEET    2   F 7 ASN A 355  MET A 368 -1  O  LEU A 362   N  THR A 302           
SHEET    3   F 7 THR A 335  GLU A 342 -1  N  THR A 340   O  THR A 361           
SHEET    4   F 7 GLN A 329  PHE A 332 -1  N  PHE A 330   O  VAL A 337           
SHEET    5   F 7 ARG A 373  GLU A 378 -1  O  ALA A 375   N  TYR A 331           
SHEET    6   F 7 ARG A 381  GLY A 393 -1  O  GLY A 386   N  PHE A 374           
SHEET    7   F 7 LYS A 299  ILE A 310 -1  N  GLU A 305   O  LYS A 390           
SHEET    1   G 2 PHE A 322  PHE A 323  0                                        
SHEET    2   G 2 MET A 349  VAL A 350 -1  O  VAL A 350   N  PHE A 322           
LINK         C   SER I 900                 N   BB9 I 901     1555   1555  1.34  
LINK         C   BB9 I 901                 N   ASN I 902     1555   1555  1.35  
LINK         C   H14 I 904                 N   BB9 I 905     1555   1555  1.35  
LINK         C   BB9 I 905                 N   TYR I 906     1555   1555  1.34  
LINK         C22 05N I 907                 N   BB9 I 908     1555   1555  1.30  
LINK         C   BB9 I 908                 N   BB9 I 909     1555   1555  1.33  
LINK         C   BB9 I 909                 N   MH6 I 910     1555   1555  1.35  
LINK         C   MH6 I 910                 N   BB9 I 911     1555   1555  1.32  
LINK         C   BB9 I 911                 N   NH2 I 912     1555   1555  1.33  
LINK         OG1 THR A  25                MG    MG A 501     1555   1555  2.25  
LINK        MG    MG A 501                 O2B GDP A 502     1555   1555  2.31  
LINK        MG    MG A 501                 O   HOH A 615     1555   1555  2.19  
LINK        MG    MG A 503                 O   HOH A 654     1555   1555  2.33  
LINK        MG    MG A 501                 O   HOH A 601     1555   1555  2.35  
LINK        MG    MG A 501                 O   HOH A 602     1555   1555  2.41  
LINK        MG    MG A 503                 O   HOH A 653     1555   1555  2.41  
LINK        MG    MG A 501                 O   HOH A 616     1555   1555  2.42  
LINK        MG    MG A 503                 O   HOH A 681     1555   1555  2.44  
LINK         C   TYR I 906                 N3  05N I 907     1555   1555  1.33  
LINK         CA  SER I 900                 C   BB9 I 909     1555   1555  1.42  
LINK         CB  SER I 900                 CB  MH6 I 910     1555   1555  1.43  
LINK         C   BB9 I 908                 SG  BB9 I 909     1555   1555  1.74  
LINK         C   SER I 900                 SG  BB9 I 901     1555   1555  1.75  
LINK         C   H14 I 904                 SG  BB9 I 905     1555   1555  1.76  
LINK         C   ASN I 902                 SG  BB6 I 903     1555   1555  1.77  
LINK         C   MH6 I 910                 SG  BB9 I 911     1555   1555  1.77  
LINK         C22 05N I 907                 SG  BB9 I 908     1555   1555  1.76  
SITE     1 AC1  7 THR A  25  CYS A  81  GDP A 502  HOH A 601                    
SITE     2 AC1  7 HOH A 602  HOH A 615  HOH A 616                               
SITE     1 AC2 19 ASP A  21  HIS A  22  GLY A  23  LYS A  24                    
SITE     2 AC2 19 THR A  25  THR A  26  PHE A  46  ASN A 135                    
SITE     3 AC2 19 LYS A 136  ASP A 138  MET A 139  SER A 173                    
SITE     4 AC2 19 ALA A 174  LEU A 175   MG A 501  HOH A 601                    
SITE     5 AC2 19 HOH A 602  HOH A 605  HOH A 615                               
SITE     1 AC3  4 GLU A 152  HOH A 653  HOH A 654  HOH A 681                    
SITE     1 AC4  5 ARG A 262  ARG A 318  HIS A 319  THR A 320                    
SITE     2 AC4  5 ARG A 381                                                     
SITE     1 AC5 18 GLU A 215  THR A 228  GLY A 257  GLU A 259                    
SITE     2 AC5 18 PHE A 261  ARG A 262  LEU A 264  ASN A 273                    
SITE     3 AC5 18 VAL A 274  GLY A 275  LEU A 277  THR A 320                    
SITE     4 AC5 18 PRO A 321  PHE A 323  LYS A 324  HOH A 672                    
SITE     5 AC5 18 HOH I1001  HOH I1002                                          
CRYST1   80.305  123.577   45.092  90.00  90.00  90.00 P 21 21 2     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012453  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.022177        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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